Unprecedented olefin-dependent histidine-kinase inhibitory of zerumbone ring-opening material
Unprecedented olefin-dependent histidine-kinase inhibitory of zerumbone ring-opening material
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DOI：
10.1016/j.bmcl.2004.08.071
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发表时间：
2004-12-06
影响因子：
2.7
通讯作者：
Okamoto, T
中科院分区：
文献类型：
--
作者：
Kitayama, T;Iwabuchi, R;Okamoto, T
Zerumbone开环衍生物4（10 E/10 Z = 3/2）抑制枯草芽孢杆菌（Bacillussubtilis）中必需组氨酸激酶YycG的自磷酸化，构成一个双组分系统（TCS）。4 E-形式的产生可以使用与4的前体形成的开环反应性的差异进行化学调节，并且分离纯4 E。立体异构体4 E主要抑制YycG的自磷酸化（IC_（50）= 63.5 μ M）。(C)2004 Elsevier Ltd.保留所有权利。
Zerumbone ring-opening derivative, 4 (l0E/10Z= 3/2), inhibited autophosphorylation of the essential histidine-kinase YycG existing in Bacillus subtilis constituting a two-component system (TCS). Generation of 4E-form could be regulated chemically using the difference from the ring-opening reactivity of the precursor forming of 4 and pure 4E was isolated. The stereoisomer, 4E, showed main inhibition activity of autophosphorylation of YycG (IC50 = 63.5 muM). (C) 2004 Elsevier Ltd. All rights reserved.